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Database: PDB
Entry: 6MYN
LinkDB: 6MYN
Original site: 6MYN 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       01-NOV-18   6MYN              
TITLE     CRYSTAL STRUCTURE OF MURINE NF-KAPPAB INDUCING KINASE (NIK) BOUND TO  
TITLE    2 INHIBITOR R7                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 14;         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: NF-KAPPA-BETA-INDUCING KINASE,SERINE/THREONINE-PROTEIN      
COMPND   5 KINASE NIK;                                                          
COMPND   6 EC: 2.7.11.25;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: MAP3K14, NIK;                                                  
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    NIK, KINASE, TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.F.HARRIS,M.SMITH,J.BARKER                                           
REVDAT   3   02-OCT-19 6MYN    1       JRNL                                     
REVDAT   2   14-AUG-19 6MYN    1       JRNL                                     
REVDAT   1   07-AUG-19 6MYN    0                                                
JRNL        AUTH   J.A.FENG,P.LEE,M.H.ALAOUI,K.BARRETT,G.CASTANEDO,R.GODEMANN,  
JRNL        AUTH 2 P.MCEWAN,X.WANG,P.WU,Y.ZHANG,S.F.HARRIS,S.T.STABEN           
JRNL        TITL   STRUCTURE BASED DESIGN OF POTENT SELECTIVE INHIBITORS OF     
JRNL        TITL 2 PROTEIN KINASE D1 (PKD1).                                    
JRNL        REF    ACS MED.CHEM.LETT.            V.  10  1260 2019              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   31531194                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.8B00658                               
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.W.FENG,P.LEE,M.H.ALAOUI,K.BARRETT,G.M.CASTANEDA,           
REMARK   1  AUTH 2 R.GODEMANN,P.MCEWAN,X.WANG,P.WU,Y.ZHANG,S.F.HARRIS,          
REMARK   1  AUTH 3 S.T.STABEN                                                   
REMARK   1  TITL   STRUCTURE BASED DESIGN OF POTENT SELECTIVE INHIBITORS OF     
REMARK   1  TITL 2 PROTEIN KINASE D1 (PKD1)                                     
REMARK   1  REF    ACS MED.CHEM.LETT.                         2019              
REMARK   1  REFN                   ISSN 1948-5875                               
REMARK   1  DOI    10.1021/ACSMEDCHEMLETT.8B0065                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.74 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.12-2829_FINAL                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.74                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.19                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 25125                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.360                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2603                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 42.1957 -  7.3111    1.00     1284   134  0.1653 0.1967        
REMARK   3     2  7.3111 -  5.8079    1.00     1201   143  0.1625 0.2088        
REMARK   3     3  5.8079 -  5.0751    1.00     1225   119  0.1627 0.2431        
REMARK   3     4  5.0751 -  4.6117    1.00     1196   125  0.1420 0.2359        
REMARK   3     5  4.6117 -  4.2815    1.00     1218   125  0.1322 0.2037        
REMARK   3     6  4.2815 -  4.0293    1.00     1173   169  0.1469 0.2172        
REMARK   3     7  4.0293 -  3.8276    1.00     1170   130  0.1605 0.2382        
REMARK   3     8  3.8276 -  3.6611    1.00     1187   130  0.1716 0.2631        
REMARK   3     9  3.6611 -  3.5202    1.00     1167   148  0.1756 0.2619        
REMARK   3    10  3.5202 -  3.3988    1.00     1183   137  0.2049 0.2953        
REMARK   3    11  3.3988 -  3.2926    1.00     1165   145  0.2075 0.2729        
REMARK   3    12  3.2926 -  3.1985    1.00     1195   119  0.2094 0.3036        
REMARK   3    13  3.1985 -  3.1143    1.00     1158   131  0.2186 0.2775        
REMARK   3    14  3.1143 -  3.0384    1.00     1207   130  0.2277 0.3394        
REMARK   3    15  3.0384 -  2.9693    1.00     1181   120  0.2309 0.3651        
REMARK   3    16  2.9693 -  2.9061    1.00     1120   164  0.2731 0.3663        
REMARK   3    17  2.9061 -  2.8480    1.00     1177   141  0.2848 0.3643        
REMARK   3    18  2.8480 -  2.7943    1.00     1170   140  0.2776 0.3853        
REMARK   3    19  2.7943 -  2.7444    1.00     1145   153  0.2902 0.3551        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.470            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.300           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 58.27                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.43                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           5301                                  
REMARK   3   ANGLE     :  1.128           7190                                  
REMARK   3   CHIRALITY :  0.057            764                                  
REMARK   3   PLANARITY :  0.007            976                                  
REMARK   3   DIHEDRAL  : 16.567           3214                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6MYN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000237851.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-AUG-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9173                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.20                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25142                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.744                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.150                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.74                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.82                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.69000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.69000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE TRIBASIC           
REMARK 280  DIHYDRATE (PH 6.2), 0.5 M AMMONIUM SULFATE, 0.9 M LITHIUM           
REMARK 280  SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       23.20500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       34.80750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       11.60250            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A   329                                                      
REMARK 465     LEU A   330                                                      
REMARK 465     GLU A   331                                                      
REMARK 465     LYS A   332                                                      
REMARK 465     VAL A   333                                                      
REMARK 465     SER A   364                                                      
REMARK 465     GLY A   365                                                      
REMARK 465     SER A   366                                                      
REMARK 465     ALA A   367                                                      
REMARK 465     LYS A   368                                                      
REMARK 465     LEU A   369                                                      
REMARK 465     GLN A   370                                                      
REMARK 465     ARG A   371                                                      
REMARK 465     LEU A   372                                                      
REMARK 465     GLY A   373                                                      
REMARK 465     PRO A   374                                                      
REMARK 465     GLU A   375                                                      
REMARK 465     THR A   376                                                      
REMARK 465     GLU A   377                                                      
REMARK 465     PRO A   545                                                      
REMARK 465     ASP A   546                                                      
REMARK 465     GLY A   547                                                      
REMARK 465     LEU A   548                                                      
REMARK 465     GLY A   549                                                      
REMARK 465     LYS A   550                                                      
REMARK 465     ALA B   329                                                      
REMARK 465     LEU B   330                                                      
REMARK 465     GLU B   331                                                      
REMARK 465     LYS B   332                                                      
REMARK 465     VAL B   333                                                      
REMARK 465     SER B   364                                                      
REMARK 465     GLY B   365                                                      
REMARK 465     SER B   366                                                      
REMARK 465     ALA B   367                                                      
REMARK 465     LYS B   368                                                      
REMARK 465     LEU B   369                                                      
REMARK 465     GLN B   370                                                      
REMARK 465     ARG B   371                                                      
REMARK 465     LEU B   372                                                      
REMARK 465     GLY B   373                                                      
REMARK 465     PRO B   374                                                      
REMARK 465     GLU B   375                                                      
REMARK 465     THR B   376                                                      
REMARK 465     GLU B   377                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A 551    OG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP A   392     NH1  ARG B   407              1.86            
REMARK 500   OD2  ASP A   536     F17  K6Y A   703              1.94            
REMARK 500   NZ   LYS A   664     O    HOH A   801              2.05            
REMARK 500   NE2  GLN A   658     O    HOH A   802              2.15            
REMARK 500   O    HOH A   831     O    HOH A   858              2.15            
REMARK 500   O    LEU B   489     O    HOH B   801              2.17            
REMARK 500   OE1  GLU A   634     NZ   LYS A   652              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TRP A 362       21.90    -76.66                                   
REMARK 500    GLU A 398       -4.18     79.60                                   
REMARK 500    GLN A 405     -155.95     53.55                                   
REMARK 500    ARG A 410       -1.82   -150.71                                   
REMARK 500    CYS A 428     -162.97   -166.75                                   
REMARK 500    ASP A 517       58.07   -154.60                                   
REMARK 500    SER A 526     -179.38    -61.04                                   
REMARK 500    ASP A 536       97.99     64.35                                   
REMARK 500    LEU A 553       58.58    -91.85                                   
REMARK 500    ASP A 556       27.21    -72.16                                   
REMARK 500    ASP A 576     -169.22   -129.33                                   
REMARK 500    TRP A 598      -31.91     76.01                                   
REMARK 500    PRO A 605      106.66    -54.20                                   
REMARK 500    PRO A 616       40.22    -70.54                                   
REMARK 500    LYS A 668       72.34   -112.95                                   
REMARK 500    PRO A 674     -168.21    -71.13                                   
REMARK 500    ASP B 392       66.09     38.18                                   
REMARK 500    VAL B 399      -61.22   -104.58                                   
REMARK 500    GLN B 405      -82.93    -38.18                                   
REMARK 500    SER B 412      -31.74    -35.43                                   
REMARK 500    SER B 450      110.77   -162.31                                   
REMARK 500    ASP B 517       52.14   -149.14                                   
REMARK 500    ASP B 536       94.89     70.58                                   
REMARK 500    LYS B 573      168.70    -46.78                                   
REMARK 500    ALA B 577       -1.90    -59.05                                   
REMARK 500    TRP B 598      -17.64     71.68                                   
REMARK 500    PRO B 605      102.89    -55.93                                   
REMARK 500    PRO B 616       45.33    -73.44                                   
REMARK 500    ALA B 625      159.38    -47.89                                   
REMARK 500    SER B 665      152.67    -42.57                                   
REMARK 500    LYS B 668      -41.55     76.93                                   
REMARK 500    PRO B 674     -168.15    -58.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K6Y A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K6Y B 704                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4G3C   RELATED DB: PDB                                   
REMARK 900 4G3C CONTAINS APO STRUCTURE OF THE SAME PROTEIN                      
DBREF  6MYN A  329   675  UNP    Q9WUL6   M3K14_MOUSE    329    675             
DBREF  6MYN B  329   675  UNP    Q9WUL6   M3K14_MOUSE    329    675             
SEQRES   1 A  347  ALA LEU GLU LYS VAL PRO VAL GLU GLU TYR LEU VAL HIS          
SEQRES   2 A  347  ALA LEU GLN GLY SER VAL SER SER GLY GLN ALA HIS SER          
SEQRES   3 A  347  LEU ALA SER LEU ALA LYS THR TRP SER SER GLY SER ALA          
SEQRES   4 A  347  LYS LEU GLN ARG LEU GLY PRO GLU THR GLU ASP ASN GLU          
SEQRES   5 A  347  GLY VAL LEU LEU THR GLU LYS LEU LYS PRO VAL ASP TYR          
SEQRES   6 A  347  GLU TYR ARG GLU GLU VAL HIS TRP MET THR HIS GLN PRO          
SEQRES   7 A  347  ARG VAL GLY ARG GLY SER PHE GLY GLU VAL HIS ARG MET          
SEQRES   8 A  347  LYS ASP LYS GLN THR GLY PHE GLN CYS ALA VAL LYS LYS          
SEQRES   9 A  347  VAL ARG LEU GLU VAL PHE ARG VAL GLU GLU LEU VAL ALA          
SEQRES  10 A  347  CYS ALA GLY LEU SER SER PRO ARG ILE VAL PRO LEU TYR          
SEQRES  11 A  347  GLY ALA VAL ARG GLU GLY PRO TRP VAL ASN ILE PHE MET          
SEQRES  12 A  347  GLU LEU LEU GLU GLY GLY SER LEU GLY GLN LEU ILE LYS          
SEQRES  13 A  347  GLN MET GLY CYS LEU PRO GLU ASP ARG ALA LEU TYR TYR          
SEQRES  14 A  347  LEU GLY GLN ALA LEU GLU GLY LEU GLU TYR LEU HIS THR          
SEQRES  15 A  347  ARG ARG ILE LEU HIS GLY ASP VAL LYS ALA ASP ASN VAL          
SEQRES  16 A  347  LEU LEU SER SER ASP GLY SER ARG ALA ALA LEU CYS ASP          
SEQRES  17 A  347  PHE GLY HIS ALA LEU CYS LEU GLN PRO ASP GLY LEU GLY          
SEQRES  18 A  347  LYS SER LEU LEU THR GLY ASP TYR ILE PRO GLY THR GLU          
SEQRES  19 A  347  THR HIS MET ALA PRO GLU VAL VAL MET GLY LYS PRO CYS          
SEQRES  20 A  347  ASP ALA LYS VAL ASP ILE TRP SER SER CYS CYS MET MET          
SEQRES  21 A  347  LEU HIS MET LEU ASN GLY CYS HIS PRO TRP THR GLN TYR          
SEQRES  22 A  347  PHE ARG GLY PRO LEU CYS LEU LYS ILE ALA SER GLU PRO          
SEQRES  23 A  347  PRO PRO ILE ARG GLU ILE PRO PRO SER CYS ALA PRO LEU          
SEQRES  24 A  347  THR ALA GLN ALA ILE GLN GLU GLY LEU ARG LYS GLU PRO          
SEQRES  25 A  347  VAL HIS ARG ALA SER ALA MET GLU LEU ARG ARG LYS VAL          
SEQRES  26 A  347  GLY LYS ALA LEU GLN GLU VAL GLY GLY LEU LYS SER PRO          
SEQRES  27 A  347  TRP LYS GLY GLU TYR LYS GLU PRO ARG                          
SEQRES   1 B  347  ALA LEU GLU LYS VAL PRO VAL GLU GLU TYR LEU VAL HIS          
SEQRES   2 B  347  ALA LEU GLN GLY SER VAL SER SER GLY GLN ALA HIS SER          
SEQRES   3 B  347  LEU ALA SER LEU ALA LYS THR TRP SER SER GLY SER ALA          
SEQRES   4 B  347  LYS LEU GLN ARG LEU GLY PRO GLU THR GLU ASP ASN GLU          
SEQRES   5 B  347  GLY VAL LEU LEU THR GLU LYS LEU LYS PRO VAL ASP TYR          
SEQRES   6 B  347  GLU TYR ARG GLU GLU VAL HIS TRP MET THR HIS GLN PRO          
SEQRES   7 B  347  ARG VAL GLY ARG GLY SER PHE GLY GLU VAL HIS ARG MET          
SEQRES   8 B  347  LYS ASP LYS GLN THR GLY PHE GLN CYS ALA VAL LYS LYS          
SEQRES   9 B  347  VAL ARG LEU GLU VAL PHE ARG VAL GLU GLU LEU VAL ALA          
SEQRES  10 B  347  CYS ALA GLY LEU SER SER PRO ARG ILE VAL PRO LEU TYR          
SEQRES  11 B  347  GLY ALA VAL ARG GLU GLY PRO TRP VAL ASN ILE PHE MET          
SEQRES  12 B  347  GLU LEU LEU GLU GLY GLY SER LEU GLY GLN LEU ILE LYS          
SEQRES  13 B  347  GLN MET GLY CYS LEU PRO GLU ASP ARG ALA LEU TYR TYR          
SEQRES  14 B  347  LEU GLY GLN ALA LEU GLU GLY LEU GLU TYR LEU HIS THR          
SEQRES  15 B  347  ARG ARG ILE LEU HIS GLY ASP VAL LYS ALA ASP ASN VAL          
SEQRES  16 B  347  LEU LEU SER SER ASP GLY SER ARG ALA ALA LEU CYS ASP          
SEQRES  17 B  347  PHE GLY HIS ALA LEU CYS LEU GLN PRO ASP GLY LEU GLY          
SEQRES  18 B  347  LYS SER LEU LEU THR GLY ASP TYR ILE PRO GLY THR GLU          
SEQRES  19 B  347  THR HIS MET ALA PRO GLU VAL VAL MET GLY LYS PRO CYS          
SEQRES  20 B  347  ASP ALA LYS VAL ASP ILE TRP SER SER CYS CYS MET MET          
SEQRES  21 B  347  LEU HIS MET LEU ASN GLY CYS HIS PRO TRP THR GLN TYR          
SEQRES  22 B  347  PHE ARG GLY PRO LEU CYS LEU LYS ILE ALA SER GLU PRO          
SEQRES  23 B  347  PRO PRO ILE ARG GLU ILE PRO PRO SER CYS ALA PRO LEU          
SEQRES  24 B  347  THR ALA GLN ALA ILE GLN GLU GLY LEU ARG LYS GLU PRO          
SEQRES  25 B  347  VAL HIS ARG ALA SER ALA MET GLU LEU ARG ARG LYS VAL          
SEQRES  26 B  347  GLY LYS ALA LEU GLN GLU VAL GLY GLY LEU LYS SER PRO          
SEQRES  27 B  347  TRP LYS GLY GLU TYR LYS GLU PRO ARG                          
HET    SO4  A 701       5                                                       
HET    SO4  A 702       5                                                       
HET    K6Y  A 703      34                                                       
HET    SO4  B 701       5                                                       
HET    SO4  B 702       5                                                       
HET    SO4  B 703       5                                                       
HET    K6Y  B 704      34                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     K6Y (5S,7S)-9-FLUORO-10-[(3R)-3-HYDROXY-3-(5-METHYL-1,2-             
HETNAM   2 K6Y  OXAZOL-3-YL)BUT-1-YN-1-YL]-N~3~-METHYL-6,7-DIHYDRO-5H-          
HETNAM   3 K6Y  5,7-METHANOIMIDAZO[2,1-A][2]BENZAZEPINE-2,3-                    
HETNAM   4 K6Y  DICARBOXAMIDE                                                   
FORMUL   3  SO4    5(O4 S 2-)                                                   
FORMUL   5  K6Y    2(C24 H22 F N5 O4)                                           
FORMUL  10  HOH   *105(H2 O)                                                    
HELIX    1 AA1 VAL A  335  GLN A  344  1                                  10    
HELIX    2 AA2 GLN A  351  LYS A  360  1                                  10    
HELIX    3 AA3 THR A  361  SER A  363  5                                   3    
HELIX    4 AA4 GLU A  436  ARG A  439  5                                   4    
HELIX    5 AA5 VAL A  440  ALA A  445  1                                   6    
HELIX    6 AA6 SER A  478  GLY A  487  1                                  10    
HELIX    7 AA7 PRO A  490  ARG A  511  1                                  22    
HELIX    8 AA8 LYS A  519  ASP A  521  5                                   3    
HELIX    9 AA9 THR A  561  MET A  565  5                                   5    
HELIX   10 AB1 ALA A  566  GLY A  572  1                                   7    
HELIX   11 AB2 ALA A  577  GLY A  594  1                                  18    
HELIX   12 AB3 PRO A  605  GLU A  613  1                                   9    
HELIX   13 AB4 PRO A  615  ILE A  620  5                                   6    
HELIX   14 AB5 ALA A  625  GLY A  635  1                                  11    
HELIX   15 AB6 SER A  645  VAL A  660  1                                  16    
HELIX   16 AB7 VAL B  335  GLN B  344  1                                  10    
HELIX   17 AB8 GLN B  351  THR B  361  1                                  11    
HELIX   18 AB9 GLU B  436  ARG B  439  5                                   4    
HELIX   19 AC1 VAL B  440  ALA B  445  1                                   6    
HELIX   20 AC2 SER B  478  GLY B  487  1                                  10    
HELIX   21 AC3 PRO B  490  ARG B  511  1                                  22    
HELIX   22 AC4 LYS B  519  ASP B  521  5                                   3    
HELIX   23 AC5 THR B  561  MET B  565  5                                   5    
HELIX   24 AC6 ALA B  566  MET B  571  1                                   6    
HELIX   25 AC7 ALA B  577  GLY B  594  1                                  18    
HELIX   26 AC8 PRO B  605  GLU B  613  1                                   9    
HELIX   27 AC9 PRO B  615  ILE B  620  5                                   6    
HELIX   28 AD1 ALA B  625  LEU B  636  1                                  12    
HELIX   29 AD2 SER B  645  VAL B  660  1                                  16    
SHEET    1 AA1 7 VAL A 347  SER A 349  0                                        
SHEET    2 AA1 7 ASN A 379  LEU A 383  1  O  LEU A 383   N  SER A 348           
SHEET    3 AA1 7 LEU A 457  GLU A 463 -1  O  ARG A 462   N  GLU A 380           
SHEET    4 AA1 7 TRP A 466  MET A 471 -1  O  ASN A 468   N  VAL A 461           
SHEET    5 AA1 7 GLN A 427  ARG A 434 -1  N  VAL A 433   O  VAL A 467           
SHEET    6 AA1 7 VAL A 416  ASP A 421 -1  N  HIS A 417   O  VAL A 430           
SHEET    7 AA1 7 TRP A 401  THR A 403 -1  N  MET A 402   O  LYS A 420           
SHEET    1 AA2 2 ILE A 513  LEU A 514  0                                        
SHEET    2 AA2 2 LEU A 541  CYS A 542 -1  O  LEU A 541   N  LEU A 514           
SHEET    1 AA3 2 VAL A 523  LEU A 525  0                                        
SHEET    2 AA3 2 ALA A 532  LEU A 534 -1  O  ALA A 533   N  LEU A 524           
SHEET    1 AA4 7 VAL B 347  SER B 349  0                                        
SHEET    2 AA4 7 ASN B 379  LEU B 383  1  O  LEU B 383   N  SER B 348           
SHEET    3 AA4 7 LEU B 457  GLU B 463 -1  O  ARG B 462   N  GLU B 380           
SHEET    4 AA4 7 TRP B 466  MET B 471 -1  O  TRP B 466   N  GLU B 463           
SHEET    5 AA4 7 GLN B 427  ARG B 434 -1  N  LYS B 431   O  ILE B 469           
SHEET    6 AA4 7 VAL B 416  ASP B 421 -1  N  HIS B 417   O  VAL B 430           
SHEET    7 AA4 7 TRP B 401  THR B 403 -1  N  MET B 402   O  LYS B 420           
SHEET    1 AA5 2 ILE B 513  LEU B 514  0                                        
SHEET    2 AA5 2 LEU B 541  CYS B 542 -1  O  LEU B 541   N  LEU B 514           
SHEET    1 AA6 2 VAL B 523  LEU B 525  0                                        
SHEET    2 AA6 2 ALA B 532  LEU B 534 -1  O  ALA B 533   N  LEU B 524           
SHEET    1 AA7 2 LYS B 550  SER B 551  0                                        
SHEET    2 AA7 2 PRO B 574  CYS B 575 -1  O  CYS B 575   N  LYS B 550           
SITE     1 AC1  4 ARG A 637  LYS A 638  GLU A 639  HOH A 810                    
SITE     1 AC2  2 ARG A 650  ARG A 651                                          
SITE     1 AC3 18 ARG A 410  GLY A 411  VAL A 416  ALA A 429                    
SITE     2 AC3 18 LYS A 431  GLU A 442  VAL A 455  ILE A 469                    
SITE     3 AC3 18 MET A 471  GLU A 472  LEU A 473  LEU A 474                    
SITE     4 AC3 18 GLY A 477  ASP A 521  LEU A 524  CYS A 535                    
SITE     5 AC3 18 ASP A 536  PHE A 537                                          
SITE     1 AC4  5 ARG B 637  LYS B 638  GLU B 639  HIS B 642                    
SITE     2 AC4  5 HOH B 813                                                     
SITE     1 AC5  2 ARG B 453  HOH B 806                                          
SITE     1 AC6  7 LYS A 519  THR A 561  HIS A 596  GLN B 351                    
SITE     2 AC6  7 HOH B 810  HOH B 815  HOH B 818                               
SITE     1 AC7 17 ARG B 410  GLY B 411  ALA B 429  LYS B 431                    
SITE     2 AC7 17 GLU B 442  VAL B 455  ILE B 469  MET B 471                    
SITE     3 AC7 17 GLU B 472  LEU B 473  LEU B 474  GLY B 477                    
SITE     4 AC7 17 ASP B 521  LEU B 524  CYS B 535  ASP B 536                    
SITE     5 AC7 17 PHE B 537                                                     
CRYST1  143.220  143.220   46.410  90.00  90.00  90.00 P 43          8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006982  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006982  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021547        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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